Export your current network:
... as a vector graphic:
SVG: scalable vector graphic - can be opened and edited in Illustrator, CorelDraw, Dia, etc
... as short tabular text output:
TSV: tab separated values - can be opened in Excel and Cytoscape (lists only one-way edges: A-B)
... as tabular text output:
TSV: tab separated values - can be opened in Excel (lists reciprocal edges: A-B,B-A)
... as an XML summary:
structured XML interaction data, according to the 'PSI-MI' data standard
... protein node degrees:
node degree of proteins in your network (given the current score cut-off)
... network coordinates:
a flat-file format describing the coordinates and colors of nodes in the network
... protein sequences:
MFA: multi-fasta format - containing the aminoacid sequences in the network
... protein annotations:
a tab-delimited file describing the names, domains and descriptions of proteins in your network
... functional annotations:
a tab-delimited file containing all known functional terms of proteins in your network
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CAZ94702.1 | CAZ94703.1 | ZOBELLIA_631 | ZOBELLIA_632 | Thrombospondin type 3 repeats protein; The presence of two EF-hand calcium-binding domains, four putatif thrombospondin type 3 repeats and one calx-beta motif suggest that this sequence is a calcium binding protein. The calx-beta motif is present in the cytoplasmic domains of Calx Na-Ca exchangers; Contains a Galactose-binding domain; Signal peptide cleaved between the residues 34 and 35; Putatively localized in the outer membrane; Conserved hypothetical protein. | Conserved hypothetical protein; Contains a signal peptide cleaved between the residues 29 and 30; Localized in the periplasmic space. | 0.873 |
| CAZ94702.1 | CAZ94709.1 | ZOBELLIA_631 | ZOBELLIA_638 | Thrombospondin type 3 repeats protein; The presence of two EF-hand calcium-binding domains, four putatif thrombospondin type 3 repeats and one calx-beta motif suggest that this sequence is a calcium binding protein. The calx-beta motif is present in the cytoplasmic domains of Calx Na-Ca exchangers; Contains a Galactose-binding domain; Signal peptide cleaved between the residues 34 and 35; Putatively localized in the outer membrane; Conserved hypothetical protein. | OmpA-like outer membrane protein; This protein has a modular architecture with two N-terminal TPR repeats, a central beta-propeller domain, encompassing five WD40 repeats, and a C-terminal OmpA domain. OmpA-like domain is thought to be responsible for non-covalent interactions with peptidoglycan. The tetratrico peptide repeat (TPR) is a structural motif, which mediates proteinprotein interactions. Signal peptide cleaved between the residues 21 and 22; Localized in the outer membrane; Function unclear. | 0.672 |
| CAZ94702.1 | CAZ94710.1 | ZOBELLIA_631 | ZOBELLIA_639 | Thrombospondin type 3 repeats protein; The presence of two EF-hand calcium-binding domains, four putatif thrombospondin type 3 repeats and one calx-beta motif suggest that this sequence is a calcium binding protein. The calx-beta motif is present in the cytoplasmic domains of Calx Na-Ca exchangers; Contains a Galactose-binding domain; Signal peptide cleaved between the residues 34 and 35; Putatively localized in the outer membrane; Conserved hypothetical protein. | Conserved hypothetical protein; Contains a signal peptide cleaved between the residues 29 and 30; Localized in the periplasmic space. | 0.701 |
| CAZ94702.1 | CAZ96561.1 | ZOBELLIA_631 | ZOBELLIA_2408 | Thrombospondin type 3 repeats protein; The presence of two EF-hand calcium-binding domains, four putatif thrombospondin type 3 repeats and one calx-beta motif suggest that this sequence is a calcium binding protein. The calx-beta motif is present in the cytoplasmic domains of Calx Na-Ca exchangers; Contains a Galactose-binding domain; Signal peptide cleaved between the residues 34 and 35; Putatively localized in the outer membrane; Conserved hypothetical protein. | Conserved hypothetical protein; Signal peptide cleaved between the residues 28 and 29; Localized in the periplasm. | 0.677 |
| CAZ94702.1 | CAZ96912.1 | ZOBELLIA_631 | ZOBELLIA_2762 | Thrombospondin type 3 repeats protein; The presence of two EF-hand calcium-binding domains, four putatif thrombospondin type 3 repeats and one calx-beta motif suggest that this sequence is a calcium binding protein. The calx-beta motif is present in the cytoplasmic domains of Calx Na-Ca exchangers; Contains a Galactose-binding domain; Signal peptide cleaved between the residues 34 and 35; Putatively localized in the outer membrane; Conserved hypothetical protein. | Conserved hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 20 and 21; Localized in the periplasmic space; Conserved hypothetical protein. | 0.714 |
| CAZ94702.1 | CAZ97043.1 | ZOBELLIA_631 | ZOBELLIA_2896 | Thrombospondin type 3 repeats protein; The presence of two EF-hand calcium-binding domains, four putatif thrombospondin type 3 repeats and one calx-beta motif suggest that this sequence is a calcium binding protein. The calx-beta motif is present in the cytoplasmic domains of Calx Na-Ca exchangers; Contains a Galactose-binding domain; Signal peptide cleaved between the residues 34 and 35; Putatively localized in the outer membrane; Conserved hypothetical protein. | Conserved hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 20 and 21; Localized in the periplasmic space; Conserved hypothetical protein. | 0.648 |
| CAZ94702.1 | CAZ97786.1 | ZOBELLIA_631 | ZOBELLIA_3648 | Thrombospondin type 3 repeats protein; The presence of two EF-hand calcium-binding domains, four putatif thrombospondin type 3 repeats and one calx-beta motif suggest that this sequence is a calcium binding protein. The calx-beta motif is present in the cytoplasmic domains of Calx Na-Ca exchangers; Contains a Galactose-binding domain; Signal peptide cleaved between the residues 34 and 35; Putatively localized in the outer membrane; Conserved hypothetical protein. | Conserved hypothetical protein; Signal peptide cleaved between the residues 20 and 21; Localized in the periplasmic space. | 0.659 |
| CAZ94702.1 | idiA | ZOBELLIA_631 | ZOBELLIA_630 | Thrombospondin type 3 repeats protein; The presence of two EF-hand calcium-binding domains, four putatif thrombospondin type 3 repeats and one calx-beta motif suggest that this sequence is a calcium binding protein. The calx-beta motif is present in the cytoplasmic domains of Calx Na-Ca exchangers; Contains a Galactose-binding domain; Signal peptide cleaved between the residues 34 and 35; Putatively localized in the outer membrane; Conserved hypothetical protein. | Isopentenyl-diphosphate Delta-isomerase is involved in isoprenoid biosynthesis. It catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl to its highly electrophilic allylic isomer, dimethylallyl diphosphate. Binds one magnesium as a cofactor when the substrate is also bound. Localized in the cytoplasm; High confidence in function and specificity. | 0.746 |
| CAZ94702.1 | pmiA | ZOBELLIA_631 | ZOBELLIA_628 | Thrombospondin type 3 repeats protein; The presence of two EF-hand calcium-binding domains, four putatif thrombospondin type 3 repeats and one calx-beta motif suggest that this sequence is a calcium binding protein. The calx-beta motif is present in the cytoplasmic domains of Calx Na-Ca exchangers; Contains a Galactose-binding domain; Signal peptide cleaved between the residues 34 and 35; Putatively localized in the outer membrane; Conserved hypothetical protein. | Mannose-6-phosphate isomerase or phosphomannose isomerase (PMI) is the enzyme that converts the mannose-6-phosphate to fructose-6-phosphate. Contains a phosphomannose isomerase type I domain; Binds 1 zinc ion per subunit; Belongs to the the cupin superfamily, mannose-6-phosphate isomerase type 1 family; Localized in the cytoplasm; High confidence in function and specificity. | 0.649 |
| CAZ94702.1 | pts | ZOBELLIA_631 | ZOBELLIA_629 | Thrombospondin type 3 repeats protein; The presence of two EF-hand calcium-binding domains, four putatif thrombospondin type 3 repeats and one calx-beta motif suggest that this sequence is a calcium binding protein. The calx-beta motif is present in the cytoplasmic domains of Calx Na-Ca exchangers; Contains a Galactose-binding domain; Signal peptide cleaved between the residues 34 and 35; Putatively localized in the outer membrane; Conserved hypothetical protein. | 6-Pyruvoyl tetrahydrobiopterin synthase is involved in the biosynthesis of tetrahydrobiopterin, an essential cofactor of aromatic amino acid hydroxylases. It catalyzes the transformation of 7,8-dihydroneopterin triphosphate into 6-pyruvoyl tetrahydropterin. It forms a homohexamer formed of two homotrimers in a head to head fashion. Localized in the cytoplasm; High confidence in function and specificity. | 0.746 |
| CAZ94703.1 | CAZ94702.1 | ZOBELLIA_632 | ZOBELLIA_631 | Conserved hypothetical protein; Contains a signal peptide cleaved between the residues 29 and 30; Localized in the periplasmic space. | Thrombospondin type 3 repeats protein; The presence of two EF-hand calcium-binding domains, four putatif thrombospondin type 3 repeats and one calx-beta motif suggest that this sequence is a calcium binding protein. The calx-beta motif is present in the cytoplasmic domains of Calx Na-Ca exchangers; Contains a Galactose-binding domain; Signal peptide cleaved between the residues 34 and 35; Putatively localized in the outer membrane; Conserved hypothetical protein. | 0.873 |
| CAZ94703.1 | CAZ94709.1 | ZOBELLIA_632 | ZOBELLIA_638 | Conserved hypothetical protein; Contains a signal peptide cleaved between the residues 29 and 30; Localized in the periplasmic space. | OmpA-like outer membrane protein; This protein has a modular architecture with two N-terminal TPR repeats, a central beta-propeller domain, encompassing five WD40 repeats, and a C-terminal OmpA domain. OmpA-like domain is thought to be responsible for non-covalent interactions with peptidoglycan. The tetratrico peptide repeat (TPR) is a structural motif, which mediates proteinprotein interactions. Signal peptide cleaved between the residues 21 and 22; Localized in the outer membrane; Function unclear. | 0.774 |
| CAZ94703.1 | CAZ96912.1 | ZOBELLIA_632 | ZOBELLIA_2762 | Conserved hypothetical protein; Contains a signal peptide cleaved between the residues 29 and 30; Localized in the periplasmic space. | Conserved hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 20 and 21; Localized in the periplasmic space; Conserved hypothetical protein. | 0.430 |
| CAZ94703.1 | idiA | ZOBELLIA_632 | ZOBELLIA_630 | Conserved hypothetical protein; Contains a signal peptide cleaved between the residues 29 and 30; Localized in the periplasmic space. | Isopentenyl-diphosphate Delta-isomerase is involved in isoprenoid biosynthesis. It catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl to its highly electrophilic allylic isomer, dimethylallyl diphosphate. Binds one magnesium as a cofactor when the substrate is also bound. Localized in the cytoplasm; High confidence in function and specificity. | 0.578 |
| CAZ94703.1 | pmiA | ZOBELLIA_632 | ZOBELLIA_628 | Conserved hypothetical protein; Contains a signal peptide cleaved between the residues 29 and 30; Localized in the periplasmic space. | Mannose-6-phosphate isomerase or phosphomannose isomerase (PMI) is the enzyme that converts the mannose-6-phosphate to fructose-6-phosphate. Contains a phosphomannose isomerase type I domain; Binds 1 zinc ion per subunit; Belongs to the the cupin superfamily, mannose-6-phosphate isomerase type 1 family; Localized in the cytoplasm; High confidence in function and specificity. | 0.503 |
| CAZ94703.1 | pts | ZOBELLIA_632 | ZOBELLIA_629 | Conserved hypothetical protein; Contains a signal peptide cleaved between the residues 29 and 30; Localized in the periplasmic space. | 6-Pyruvoyl tetrahydrobiopterin synthase is involved in the biosynthesis of tetrahydrobiopterin, an essential cofactor of aromatic amino acid hydroxylases. It catalyzes the transformation of 7,8-dihydroneopterin triphosphate into 6-pyruvoyl tetrahydropterin. It forms a homohexamer formed of two homotrimers in a head to head fashion. Localized in the cytoplasm; High confidence in function and specificity. | 0.573 |
| CAZ94709.1 | CAZ94702.1 | ZOBELLIA_638 | ZOBELLIA_631 | OmpA-like outer membrane protein; This protein has a modular architecture with two N-terminal TPR repeats, a central beta-propeller domain, encompassing five WD40 repeats, and a C-terminal OmpA domain. OmpA-like domain is thought to be responsible for non-covalent interactions with peptidoglycan. The tetratrico peptide repeat (TPR) is a structural motif, which mediates proteinprotein interactions. Signal peptide cleaved between the residues 21 and 22; Localized in the outer membrane; Function unclear. | Thrombospondin type 3 repeats protein; The presence of two EF-hand calcium-binding domains, four putatif thrombospondin type 3 repeats and one calx-beta motif suggest that this sequence is a calcium binding protein. The calx-beta motif is present in the cytoplasmic domains of Calx Na-Ca exchangers; Contains a Galactose-binding domain; Signal peptide cleaved between the residues 34 and 35; Putatively localized in the outer membrane; Conserved hypothetical protein. | 0.672 |
| CAZ94709.1 | CAZ94703.1 | ZOBELLIA_638 | ZOBELLIA_632 | OmpA-like outer membrane protein; This protein has a modular architecture with two N-terminal TPR repeats, a central beta-propeller domain, encompassing five WD40 repeats, and a C-terminal OmpA domain. OmpA-like domain is thought to be responsible for non-covalent interactions with peptidoglycan. The tetratrico peptide repeat (TPR) is a structural motif, which mediates proteinprotein interactions. Signal peptide cleaved between the residues 21 and 22; Localized in the outer membrane; Function unclear. | Conserved hypothetical protein; Contains a signal peptide cleaved between the residues 29 and 30; Localized in the periplasmic space. | 0.774 |
| CAZ94709.1 | CAZ94710.1 | ZOBELLIA_638 | ZOBELLIA_639 | OmpA-like outer membrane protein; This protein has a modular architecture with two N-terminal TPR repeats, a central beta-propeller domain, encompassing five WD40 repeats, and a C-terminal OmpA domain. OmpA-like domain is thought to be responsible for non-covalent interactions with peptidoglycan. The tetratrico peptide repeat (TPR) is a structural motif, which mediates proteinprotein interactions. Signal peptide cleaved between the residues 21 and 22; Localized in the outer membrane; Function unclear. | Conserved hypothetical protein; Contains a signal peptide cleaved between the residues 29 and 30; Localized in the periplasmic space. | 0.943 |
| CAZ94709.1 | CAZ96561.1 | ZOBELLIA_638 | ZOBELLIA_2408 | OmpA-like outer membrane protein; This protein has a modular architecture with two N-terminal TPR repeats, a central beta-propeller domain, encompassing five WD40 repeats, and a C-terminal OmpA domain. OmpA-like domain is thought to be responsible for non-covalent interactions with peptidoglycan. The tetratrico peptide repeat (TPR) is a structural motif, which mediates proteinprotein interactions. Signal peptide cleaved between the residues 21 and 22; Localized in the outer membrane; Function unclear. | Conserved hypothetical protein; Signal peptide cleaved between the residues 28 and 29; Localized in the periplasm. | 0.775 |
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